Affinity Labelling of Yeast Phenylalanyl‐tRNA Synthetase with a 37′‐Oxidised tRNAPhe
Open Access
- 1 April 1982
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 123 (2) , 267-274
- https://doi.org/10.1111/j.1432-1033.1982.tb19763.x
Abstract
Yeast phenylalanyl-tRNA synthetase was specifically labeled with a 3''-oxidized tRNAPhe. Stoichiometric inactivation was achieved with the incorporation of 2 mol oxidized tRNAPhe/mol enzyme which corresponds exactly to the stoichiometry of tRNA binding. The labeled peptide was isolated using a quick chromatographic procedure which can be applied to any covalent complex formed between a tRNA and an aminoacyl-tRNA synthetase. The isolated peptide (18 amino acids) encompassed the unique cysteine sequence of the smaller .beta. subunit of the enzyme.This publication has 21 references indexed in Scilit:
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